|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
16-658 |
0e+00 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 745.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 16 QGDYIPRQVQTWTKQYRAA----ETSSIPAMERLIQWLPLHLPRQQ----RTTLVHGDFRLDNLIFHPEKAEVLAVLDWE 87
Cdd:PLN02876 174 RDNYCKRQVERWAKQYLAStgegKPPRNPKMLELIDWLRENIPAEDstgaGTGIVHGDFRIDNLVFHPTEDRVIGILDWE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 88 LSTLGDPFADVAYSCLAYYLPSSFP---ILRGFRDQDVTKlGIPTVEEYFRMYCLNMGIP-PIDNWNFYMAFSFFRVAAI 163
Cdd:PLN02876 254 LSTLGNQMCDVAYSCLPYIVDINLDnqqVGKGFEFTGIPE-GIPSLPEYLAEYCSASGKPwPAANWKFYVAFSLFRGASI 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 164 LQGVYKRSLTGQASSAT-AQQSGKLTESMAELAWDFATKEGfrVFKEMPatktlsrsyhawagprsprtPKGVRGHStvA 242
Cdd:PLN02876 333 YAGVYSRWLMGNASGGErARNAGKQANFLVDSALDYIARKN--VLPEHP--------------------PSGQFGRE--P 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 243 AASPSHEAKGGLVISPEglspaVRKLYEQLVQFIEQKVYPLEPELQRHQASADRWSPSPLIEDLKEKAKAEGLWNLFLPL 322
Cdd:PLN02876 389 EYSSLSKESGRFVPSEK-----VLELRKKLIKFMEDHIYPMENEFYKLAQSSSRWTVHPEEERLKELAKKEGLWNLWIPL 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 323 ET-------------------DPEKKYGAGLTNVEYAHLCEVMGMSLYASEIFNCSAPDTGNMEILVRYGTEEQKARWLV 383
Cdd:PLN02876 464 DSaararkllfednkhmvsgdSADQLLGAGLSNLEYGYLCEIMGRSVWAPQVFNCGAPDTGNMEVLLRYGNKEQQLEWLI 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 384 PLLEGRIRSCFAMTEPQVASSDASNIEASIKEEDGCYVINGHKWWTSGILDPRCKLCVFMGKTDPQAPRHQQQSMLLVPM 463
Cdd:PLN02876 544 PLLEGKIRSGFAMTEPQVASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVMGKTDFNAPKHKQQSMILVDI 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 464 DSPGITVIRPLSVFGLEDPPGGHGEVRFKDVRVPKENILLGPGRGFEIAQGRLGPGRIHHCMRLIGYSERALALMKTRVM 543
Cdd:PLN02876 624 QTPGVQIKRPLLVFGFDDAPHGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRAL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 544 SRTAFGKPLVEQGTILADIARSRVEIEQARLLVLKAAHLMDVAGNKTAALDIAMIKMVVPSMAYHVIDRAIQAFGAAGLS 623
Cdd:PLN02876 704 SRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRLGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVS 783
|
650 660 670
....*....|....*....|....*....|....*
gi 1720414863 624 SDYPLAQFFGWARALRFADGPDEVHQLTVAKMELK 658
Cdd:PLN02876 784 SDTVLAHLWATARTLRIADGPDEVHLGTIAKLELQ 818
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
265-658 |
0e+00 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 652.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 265 VRKLYEQLVQFIEQKVYPLEPELQRHQASADR--WSPSPLIEDLKEKAKAEGLWNLFLPletdpEKKYGAGLTNVEYAHL 342
Cdd:cd01155 3 AQELRARVKAFMEEHVYPAEQEFLEYYAEGGDrwWTPPPIIEKLKAKAKAEGLWNLFLP-----EVSGLSGLTNLEYAYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 343 CEVMGMSLYASEIFNCSAPDTGNMEILVRYGTEEQKARWLVPLLEGRIRSCFAMTEPQVASSDASNIEASIKEEDGCYVI 422
Cdd:cd01155 78 AEETGRSFFAPEVFNCQAPDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASSDATNIECSIERDGDDYVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 423 NGHKWWTSGILDPRCKLCVFMGKTDP-QAPRHQQQSMLLVPMDSPGITVIRPLSVFGLEDPPGGHGEVRFKDVRVPKENI 501
Cdd:cd01155 158 NGRKWWSSGAGDPRCKIAIVMGRTDPdGAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHGHAEITFDNVRVPASNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 502 LLGPGRGFEIAQGRLGPGRIHHCMRLIGYSERALALMKTRVMSRTAFGKPLVEQGTILADIARSRVEIEQARLLVLKAAH 581
Cdd:cd01155 238 ILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAH 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720414863 582 LMDVAGNKTAALDIAMIKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALRFADGPDEVHQLTVAKMELK 658
Cdd:cd01155 318 MIDTVGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
261-658 |
5.01e-110 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 337.20 E-value: 5.01e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 261 LSPAVRKLYEQLVQFIEQKVYPLEPELQRHQAsadrwspspLIEDLKEKAKAEGLWNLFLPletdpeKKY-GAGLTNVEY 339
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGE---------FPRELWRKLAELGLLGLTIP------EEYgGLGLSLVEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 340 AHLCEVMGMSLyASEIFNCSAPDtGNMEILVRYGTEEQKARWLVPLLEGRIRSCFAMTEPQvASSDASNIEASIKEEDGC 419
Cdd:COG1960 70 ALVLEELARAD-ASLALPVGVHN-GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPG-AGSDAAALRTTAVRDGDG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 420 YVINGHKWWTSGIldPRCKLCVFMGKTDPqAPRHQQQSMLLVPMDSPGITVIRPLSVFGLedPPGGHGEVRFKDVRVPKE 499
Cdd:COG1960 147 YVLNGQKTFITNA--PVADVILVLARTDP-AAGHRGISLFLVPKDTPGVTVGRIEDKMGL--RGSDTGELFFDDVRVPAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 500 NILLGPGRGFEIAQGRLGPGRIHHCMRLIGYSERALALMKTRVMSRTAFGKPLVEQGTILADIARSRVEIEQARLLVLKA 579
Cdd:COG1960 222 NLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRA 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720414863 580 AHLMDVAgnKTAALDIAMIKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALRFADGPDEVHQLTVAKMELK 658
Cdd:COG1960 302 AWLLDAG--EDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
362-654 |
2.16e-86 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 273.78 E-value: 2.16e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 362 DTGNMEILVRYGTEEQKARWLVPLLEGRIRSCFAMTEPQvASSDASNIEASIKEEDGCYVINGHKWWTSGIldPRCKLCV 441
Cdd:cd00567 41 LLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPG-AGSDLAGIRTTARKDGDGYVLNGRKIFISNG--GDADLFI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 442 FMGKTDPQAPRHQQQSMLLVPMDSPGITVIRPLSVFGLEdpPGGHGEVRFKDVRVPKENILLGPGRGFEIAQGRLGPGRI 521
Cdd:cd00567 118 VLARTDEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMR--GSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 522 HHCMRLIGYSERALALMKTRVMSRTAFGKPLVEQGTILADIARSRVEIEQARLLVLKAAHLMDvAGNKTAALDIAMIKMV 601
Cdd:cd00567 196 LLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLD-QGPDEARLEAAMAKLF 274
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1720414863 602 VPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALRFADGPDEVHQLTVAK 654
Cdd:cd00567 275 ATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
326-658 |
1.34e-53 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 188.25 E-value: 1.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 326 PEKKYGAGLTNVEYAhLC--EVMGMSLYASEIfnCSAPDTGNMEILVRYGTEEQKARWLVPLLEGRIRSCFAMTEPqVAS 403
Cdd:cd01158 50 PEEYGGAGLDFLAYA-IAieELAKVDASVAVI--VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEP-GAG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 404 SDASNIEASIKEEDGCYVINGHKWWTS--GILDprckLCVFMGKTDPQApRHQQQSMLLVPMDSPGITVIRPlsvfglED 481
Cdd:cd01158 126 SDAAALKTTAKKDGDDYVLNGSKMWITngGEAD----FYIVFAVTDPSK-GYRGITAFIVERDTPGLSVGKK------ED 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 482 PPGGHG----EVRFKDVRVPKENILLGPGRGFEIAQGRLGPGRIHHCMRLIGYSERALALMKTRVMSRTAFGKPLVEQGT 557
Cdd:cd01158 195 KLGIRGssttELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 558 ILADIARSRVEIEQARLLVLKAAHLMDvAGnKTAALDIAMIKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARA 637
Cdd:cd01158 275 IQFKLADMATEIEAARLLTYKAARLKD-NG-EPFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKI 352
|
330 340
....*....|....*....|.
gi 1720414863 638 LRFADGPDEVHQLTVAKMELK 658
Cdd:cd01158 353 TEIYEGTSEIQRLVIAKHLLK 373
|
|
| ACAD10_11_N-like |
cd05154 |
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ... |
17-138 |
4.79e-43 |
|
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).
Pssm-ID: 270703 [Multi-domain] Cd Length: 254 Bit Score: 155.85 E-value: 4.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 17 GDYIPRQVQTWTKQYRAAETSSIPAMERLIQWLPLHLPRQQRTTLVHGDFRLDNLIFHPEkAEVLAVLDWELSTLGDPFA 96
Cdd:cd05154 135 EGYLERQVDRWRRQLEAAATDPPPALEEALRWLRANLPADGRPVLVHGDFRLGNLLFDPD-GRVTAVLDWELATLGDPLE 213
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1720414863 97 DVAYSCLAYYLPSSFPILRGFRDQDvtklGIPTVEEYFRMYC 138
Cdd:cd05154 214 DLAWLLARWWRPGDPPGLAAPTRLP----GFPSREELLARYE 251
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
368-654 |
4.10e-41 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 154.04 E-value: 4.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 368 ILVRYGTEEQKARWLVPLLEGRIRSCFAMTEPQvASSDASNIEASIKEEDGCYVINGHKWWTSGI-LDPRCKLCVfmgKT 446
Cdd:cd01152 95 TILAYGTDEQKRRFLPPILSGEEIWCQGFSEPG-AGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAhYADWAWLLV---RT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 447 DPQAPRHQQQSMLLVPMDSPGITViRPL-SVFGLEDppggHGEVRFKDVRVPKENILLGPGRGFEIAQGRLGPGRihhcM 525
Cdd:cd01152 171 DPEAPKHRGISILLVDMDSPGVTV-RPIrSINGGEF----FNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFER----V 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 526 RLIGYSERALALMKTRVMSRTAFGKPLVEQGTILADIARSRVEIEQARLLVLKAAHLMdvAGNKTAALDIAMIKMVVPSM 605
Cdd:cd01152 242 SIGGSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASAL--AAGKPPGAEASIAKLFGSEL 319
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720414863 606 AYHVIDRAIQAFGAAGLSSDYPLAQFFG--------WARALRFADGPDEVHQLTVAK 654
Cdd:cd01152 320 AQELAELALELLGTAALLRDPAPGAELAgrweadylRSRATTIYGGTSEIQRNIIAE 376
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
258-659 |
8.77e-39 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 148.39 E-value: 8.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 258 PEGLSPAVRKLYEQLV----QFIEQKVYPLE-PELQRHQasadrwspspliEDLKEKAKAEGLWNLFLPLETDpekkyGA 332
Cdd:cd01161 20 PSVLTEEQTEELNMLVgpveKFFEEVNDPAKnDQLEKIP------------RKTLTQLKELGLFGLQVPEEYG-----GL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 333 GLTNVEYAHLCEVMGMSLYASEIFNCSApDTGNMEILVrYGTEEQKARWLVPLLEGRIRSCFAMTEPQvASSDASNIEAS 412
Cdd:cd01161 83 GLNNTQYARLAEIVGMDLGFSVTLGAHQ-SIGFKGILL-FGTEAQKEKYLPKLASGEWIAAFALTEPS-SGSDAASIRTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 413 -IKEEDG-CYVINGHKWWTS--GILDprcKLCVFmGKT---DPQAPRHQQQSMLLVPMDSPGITVIRPlsvfglEDPPGG 485
Cdd:cd01161 160 aVLSEDGkHYVLNGSKIWITngGIAD---IFTVF-AKTevkDATGSVKDKITAFIVERSFGGVTNGPP------EKKMGI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 486 HG----EVRFKDVRVPKENILLGPGRGFEIAQGRLGPGRIHHCMRLIGYSERALALMKTRVMSRTAFGKPLVEQGTILAD 561
Cdd:cd01161 230 KGsntaEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 562 IARSRVEIEQARLLVLKAAHLMDVAGNKTAALDIAMIKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALRFA 641
Cdd:cd01161 310 LANMAILQYATESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIF 389
|
410
....*....|....*...
gi 1720414863 642 DGPDEVHQLTVAKMELKN 659
Cdd:cd01161 390 EGTNEILRLFIALTGLQH 407
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
274-654 |
2.61e-38 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 146.11 E-value: 2.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 274 QFIEQKVYPLepelqrhqasADRWSPSPLIE-DLKEKAKAEGLWNLFLPLEtdpekkYGAGLTNVEYAhlcevmgmSLYA 352
Cdd:cd01160 12 RFFAKEVAPF----------HHEWEKAGEVPrEVWRKAGEQGLLGVGFPEE------YGGIGGDLLSA--------AVLW 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 353 SEI--FNCSAP------DTGnMEILVRYGTEEQKARWLVPLLEGRIRSCFAMTEPQvASSDASNIEASIKEEDGCYVING 424
Cdd:cd01160 68 EELarAGGSGPglslhtDIV-SPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPG-AGSDLQGIRTTARKDGDHYVLNG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 425 HKWW-TSGIldpRCKLCVFMGKTDPQAPRHQQQSMLLVPMDSPGITVIRPLSVFGLEdpPGGHGEVRFKDVRVPKENILL 503
Cdd:cd01160 146 SKTFiTNGM---LADVVIVVARTGGEARGAGGISLFLVERGTPGFSRGRKLKKMGWK--AQDTAELFFDDCRVPAENLLG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 504 GPGRGFEIAQGRLGPGRIHHCMRLIGYSERALALMKTRVMSRTAFGKPLVEQGTILADIARSRVEIEQARLLVLKAAHLm 583
Cdd:cd01160 221 EENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWR- 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720414863 584 DVAGnKTAALDIAMIKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALRFADGPDEVHQLTVAK 654
Cdd:cd01160 300 HEQG-RLDVAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
371-657 |
2.62e-37 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 143.35 E-value: 2.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 371 RYGTEEQKARWLVPLLEGRIRSCFAMTEPQvASSDASNIEASIKEEDGCYVINGHKWWTSGILDPrcKLCVFMGKTDPQA 450
Cdd:cd01162 95 SFGNDEQRERFLPDLCTMEKLASYCLTEPG-SGSDAAALRTRAVREGDHYVLNGSKAFISGAGDS--DVYVVMARTGGEG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 451 PRhqQQSMLLVPMDSPGITvirplsvFGL-EDPPGGHGE----VRFKDVRVPKENILLGPGRGFEIAQGRLGPGRIHHCM 525
Cdd:cd01162 172 PK--GISCFVVEKGTPGLS-------FGAnEKKMGWNAQptraVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIAS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 526 RLIGYSERALALMKTRVMSRTAFGKPLVEQGTI---LADIArsrVEIEQARLLVLKAAHLMDvAGNKTAALDIAMIKMVV 602
Cdd:cd01162 243 CSLGAAQAALDLARAYLEERKQFGKPLADFQALqfkLADMA---TELVASRLMVRRAASALD-RGDPDAVKLCAMAKRFA 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1720414863 603 PSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALRFADGPDEVHQLTVAKMEL 657
Cdd:cd01162 319 TDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALL 373
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
506-654 |
7.15e-37 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 134.69 E-value: 7.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 506 GRGFEIAQGRLGPGRIHHCMRLIGYSERALALMKTRVMSRTAFGKPLVEQGTILADIARSRVEIEQARLLVLKAAHLMDV 585
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720414863 586 AGNKTAAldIAMIKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALRFADGPDEVHQLTVAK 654
Cdd:pfam00441 81 GGPDGAE--ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
261-657 |
4.53e-34 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 133.87 E-value: 4.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 261 LSPAVRKLYEQLVQFIEQKVYPLEPELQRHQASadrwsPSPLIEdlkeKAKAEGLWNLFLPletdpEKKYGAGLTNVEYA 340
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEY-----PWPLIK----RAWELGLMNTHIP-----EDCGGLGLGTFDTC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 341 HLCEVMGmslyaseiFNCS-------APDTGNMEILVRyGTEEQKARWLVPLLEGRIRSCFAMTEPQvASSDASNIEASI 413
Cdd:cd01157 67 LITEELA--------YGCTgvqtaieANSLGQMPVIIS-GNDEQKKKYLGRMTEEPLMCAYCVTEPG-AGSDVAGIKTKA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 414 KEEDGCYVINGHKWWTSGILDPRCKLCVFMGKTDPQAPRHQQQSMLLVPMDSPGITVIRPLSVFG--LEDPPGghgeVRF 491
Cdd:cd01157 137 EKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGqrCSDTRG----ITF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 492 KDVRVPKENILLGPGRGFEIAQGRLGPGRIHHCMRLIGYSERALALMKTRVMSRTAFGKPLVEQGTI---LADIArsrVE 568
Cdd:cd01157 213 EDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVsfmLADMA---MK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 569 IEQARLLVLKAAHLMDVAGNKTAALDIAmiKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALRFADGPDEVH 648
Cdd:cd01157 290 VELARLAYQRAAWEVDSGRRNTYYASIA--KAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQ 367
|
....*....
gi 1720414863 649 QLTVAKMEL 657
Cdd:cd01157 368 RLIISREHL 376
|
|
| YcbJ |
COG3173 |
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ... |
22-154 |
2.60e-31 |
|
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];
Pssm-ID: 442406 [Multi-domain] Cd Length: 284 Bit Score: 123.69 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 22 RQVQTWTKQYRAA--ETSSIPAM-ERLIQWLPLHLPRQQRTTLVHGDFRLDNLIFHPEKAEVLAVLDWELSTLGDPFADV 98
Cdd:COG3173 152 RQLARWRAQLRRAlaRTDDLPALrERLAAWLAANLPEWGPPVLVHGDLRPGNLLVDPDDGRLTAVIDWELATLGDPAADL 231
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720414863 99 AYSCLAYYLPSSFPILRgfrdqdvtklgiptvEEYFRMYCLNMGipPIDNWNFYMA 154
Cdd:COG3173 232 AYLLLYWRLPDDLLGPR---------------AAFLAAYEEATG--DLDDLTWWAL 270
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
343-647 |
5.59e-29 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 119.06 E-value: 5.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 343 CEVMGMSLYASEIFNCSAP-----DTGNMEILVRYGTEEQKARWLVPLLE-GRIRSCFAMTEPQvASSDASNIEASIKEE 416
Cdd:PRK12341 65 ADYVTQMLVLEEVSKCGAPaflitNGQCIHSMRRFGSAEQLRKTAESTLEtGDPAYALALTEPG-AGSDNNSATTTYTRK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 417 DGCYVINGHKWWTSGILDPRCKLCVfmgKTDPQAP-RHQQQSMLLVPMDSPGITvIRPLSVFGledppgGH----GEVRF 491
Cdd:PRK12341 144 NGKVYLNGQKTFITGAKEYPYMLVL---ARDPQPKdPKKAFTLWWVDSSKPGIK-INPLHKIG------WHmlstCEVYL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 492 KDVRVPKENILLGPGRGFEIAQGRLGPGRIHHCMRLIGYSERALALMKTRVMSRTAFGKPLVEQGTILADIARSRVEIEQ 571
Cdd:PRK12341 214 DNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIEN 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720414863 572 ARLLVLKAAHLMDvaGNKTAALDIAMIKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALRFADGPDEV 647
Cdd:PRK12341 294 MRNMVYKVAWQAD--NGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEI 367
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
260-654 |
1.26e-27 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 115.20 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 260 GLSPAVRKLYEQLVQFIEQKVYPLEPELQR-HQASADRWspspliedlkEKAKAEGLWNLflpleTDPEKKYGAGLTNVE 338
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRdNEFPRDLW----------RKMGKLGLLGI-----TAPEEYGGSGMGYLA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 339 YAHLCEVMGmslYASEIFNCSAPDTGNMEI--LVRYGTEEQKARWLVPLLEGRIRSCFAMTEPQvASSDASNIEASIKEE 416
Cdd:cd01156 66 HVIIMEEIS---RASGSVALSYGAHSNLCInqIYRNGSAAQKEKYLPKLISGEHIGALAMSEPN-AGSDVVSMKLRAEKK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 417 DGCYVINGHKWW-TSGildPRCKLCVFMGKTDPQAPRHQQQSmLLVPMDSPGITVIRPLSVFGLEDPPGghGEVRFKDVR 495
Cdd:cd01156 142 GDRYVLNGSKMWiTNG---PDADTLVVYAKTDPSAGAHGITA-FIVEKGMPGFSRAQKLDKLGMRGSNT--CELVFEDCE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 496 VPKENILLGPGRGFEIAQGRLGPGRIHHCMRLIGYSERALALMKTRVMSRTAFGKPLVEQGTILADIARSRVEIEQARLL 575
Cdd:cd01156 216 VPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSY 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720414863 576 VLKAAHLMDvAGNKTaALDIAMIKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALRFADGPDEVHQLTVAK 654
Cdd:cd01156 296 LYTVAKACD-RGNMD-PKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGR 372
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
374-658 |
1.51e-23 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 103.48 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 374 TEEQKARWLVPLLEGRIRSCFAMTEPQVASSDASNIEASIKEEDGCYVINGHKWW-TSGILdprCKLCVFMGKTDPQApr 452
Cdd:PTZ00461 135 SPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKIWiTNGTV---ADVFLIYAKVDGKI-- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 453 hqqqSMLLVPMDSPGITVIRPLSVFGLEdppGGH-GEVRFKDVRVPKENILLGPGRGFEIAQGRLGPGRIHHCMRLIGYS 531
Cdd:PTZ00461 210 ----TAFVVERGTKGFTQGPKIDKCGMR---ASHmCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 532 ERALALMKTRVMSRTAFGKPLVEQGTILADIARSRVEIEQARLLVLKAAHLMDVAGNKTAALDIAmiKMVVPSMAYHVID 611
Cdd:PTZ00461 283 ERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAA--KLFATPIAKKVAD 360
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1720414863 612 RAIQAFGAAGLSSDYPLAQFFGWARALRFADGPDEVHQLTVAKMELK 658
Cdd:PTZ00461 361 SAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLK 407
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
264-654 |
3.12e-23 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 102.44 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 264 AVRKLYEQlvqFIEQKVYPLEPELQRHQASadrwsPSPLIEDLKEkakaeglwnlfLPLETDPEKKYG-AGLTNVEYAHL 342
Cdd:cd01151 19 AIRDTARE---FCQEELAPRVLEAYREEKF-----DRKIIEEMGE-----------LGLLGATIKGYGcAGLSSVAYGLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 343 C-EVMGM-SLYASEIfncSAPDTGNMEILVRYGTEEQKARWLVPLLEGRIRSCFAMTEPQvASSDASNIEASIKEEDGCY 420
Cdd:cd01151 80 ArEVERVdSGYRSFM---SVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPN-HGSDPGGMETRARKDGGGY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 421 VINGHKWWTSGilDPRCKLCVFMGKTDpqapRHQQQSMLLVPMDSPGITVIRPLSVFGLEDPPggHGEVRFKDVRVPKEN 500
Cdd:cd01151 156 KLNGSKTWITN--SPIADVFVVWARND----ETGKIRGFILERGMKGLSAPKIQGKFSLRASI--TGEIVMDNVFVPEEN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 501 ILlgPGrgfeiAQGRLGPGRIHHCMRL------IGYSERALALMKTRVMSRTAFGKPLVEQGTILADIARSRVEIEQARL 574
Cdd:cd01151 228 LL--PG-----AEGLRGPFKCLNNARYgiawgaLGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 575 LVLKAAHLMDVAgnKTAALDIAMIKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALRFADGPDEVHQLTVAK 654
Cdd:cd01151 301 ACLRVGRLKDQG--KATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGR 378
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
299-643 |
1.59e-21 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 97.46 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 299 PSPLIEDLKEKAKAeGLWNLFLPletdpEKKYGAGLTNVEYAHLCEVM--GMSlYASEIFNCsapdTGNMEILVRYGTEE 376
Cdd:cd01153 35 PPPFKEALDAFAEA-GWMALGVP-----EEYGGQGLPITVYSALAEIFsrGDA-PLMYASGT----QGAAATLLAHGTEA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 377 QKARWLVPLLEGRIRSCFAMTEPQvASSDASNIEA-SIKEEDGCYVINGHKWWTS---GILDPRCKLCVfMGKTDPQAPR 452
Cdd:cd01153 104 QREKWIPRLAEGEWTGTMCLTEPD-AGSDLGALRTkAVYQADGSWRINGVKRFISageHDMSENIVHLV-LARSEGAPPG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 453 HQQQSMLLVPMDSPGITViRPLSVFGLEDPPGGHG----EVRFKDVRVPkeniLLG-PGRG----FEIAQG-RLGPGrih 522
Cdd:cd01153 182 VKGLSLFLVPKFLDDGER-NGVTVARIEEKMGLHGsptcELVFDNAKGE----LIGeEGMGlaqmFAMMNGaRLGVG--- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 523 hcMRLIGYSERALALMKTRVMSRTAFGKPLVEQG--TIL--ADIARS----RVEIEQARLLVLKAAHLMDVAGNKTAALD 594
Cdd:cd01153 254 --TQGTGLAEAAYLNALAYAKERKQGGDLIKAAPavTIIhhPDVRRSlmtqKAYAEGSRALDLYTATVQDLAERKATEGE 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720414863 595 IA------------MIKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALRFADG 643
Cdd:cd01153 332 DRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEG 392
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
270-660 |
3.02e-21 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 96.48 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 270 EQLVQFIEQKVYPlepelqrHQASADRWSPSPliedlkekaKAEGLWNLF----LPLETDPEKKYGAGLTnveYAHLCEV 345
Cdd:PLN02519 35 ESVQQFAQENIAP-------HAAAIDATNSFP---------KDVNLWKLMgdfnLHGITAPEEYGGLGLG---YLYHCIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 346 MGMSLYASEIFNCSAPDTGNMEI--LVRYGTEEQKARWLVPLLEGRIRSCFAMTEPQvASSDASNIEASIKEEDGCYVIN 423
Cdd:PLN02519 96 MEEISRASGSVGLSYGAHSNLCInqLVRNGTPAQKEKYLPKLISGEHVGALAMSEPN-SGSDVVSMKCKAERVDGGYVLN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 424 GHKWW-TSGildPRCKLCVFMGKTDPQAPRHqQQSMLLVPMDSPGITVIRPLSVFGLEDppGGHGEVRFKDVRVPKENIL 502
Cdd:PLN02519 175 GNKMWcTNG---PVAQTLVVYAKTDVAAGSK-GITAFIIEKGMPGFSTAQKLDKLGMRG--SDTCELVFENCFVPEENVL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 503 LGPGRGFEIAQGRLGPGRIHHCMRLIGYSERALALMKTRVMSRTAFGKPLVEQGTILADIARSRVEIEQARLLVLKAAHL 582
Cdd:PLN02519 249 GQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARD 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720414863 583 MDvaGNKTAALDIAMIKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALRFADGPDEVHQLTVAKMELKNQ 660
Cdd:PLN02519 329 CD--NGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKEE 404
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
393-492 |
1.43e-20 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 86.57 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 393 CFAMTEPQvASSDASNIEASIKEEDG-CYVINGHKWWTSGIldPRCKLCVFMGKTDpQAPRHQQQSMLLVPMDSPGITVI 471
Cdd:pfam02770 1 AFALTEPG-AGSDVASLKTTAADGDGgGWVLNGTKWWITNA--GIADLFLVLARTG-GDDRHGGISLFLVPKDAPGVSVR 76
|
90 100
....*....|....*....|.
gi 1720414863 472 RPLSVFGLEDPPggHGEVRFK 492
Cdd:pfam02770 77 RIETKLGVRGLP--TGELVFD 95
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
284-652 |
1.21e-19 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 92.05 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 284 EPELQRHQASADR----WSPSPLIEdLKEKAKAEGLWNL--FLPLETDPEKKYGAG--LTNVEYAHLCEV-MGM-SLYAs 353
Cdd:cd01154 45 PPVLEMWDRWGRRvdrvWVHPAWHA-LMRRLIEEGVINIedGPAGEGRRHVHFAAGylLSDAAAGLLCPLtMTDaAVYA- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 354 eifncsapdtgnmeiLVRYGTEEQKaRWLVPLLEGRIR----SCFAMTEPQVASSDASNIEASIKEEDGCYVINGHKWWT 429
Cdd:cd01154 123 ---------------LRKYGPEELK-QYLPGLLSDRYKtgllGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 430 SGILdprCKLCVFMGKTDPQAPRHQQQSMLLVPMDSP-----GITVIRplsvfgLEDPPGGH----GEVRFKDVrvpkEN 500
Cdd:cd01154 187 SAPL---ADAALVLARPEGAPAGARGLSLFLVPRLLEdgtrnGYRIRR------LKDKLGTRsvatGEVEFDDA----EA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 501 ILLGP-GRGFEIAQGRLGPGRIHHCMRLIGYSERALALMKTRVMSRTAFGKPLVEQGTILADIARSRVEIEQARLLVLKA 579
Cdd:cd01154 254 YLIGDeGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRA 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720414863 580 AHLMDVAGN------KTAALDIAMIKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALRFADGPDEVHQLTV 652
Cdd:cd01154 334 ARAFDRAAAdkpveaHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDV 412
|
|
| APH |
pfam01636 |
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ... |
19-119 |
1.35e-17 |
|
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.
Pssm-ID: 426359 [Multi-domain] Cd Length: 239 Bit Score: 82.55 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 19 YIPRQVQTWTKQYRAAET-SSIPAM-ERLIQWLPLHLPRQQRTTLVHGDFRLDNLIFHPEKaEVLAVLDWELSTLGDPFA 96
Cdd:pfam01636 125 ELLRQLEAALARLLAAELlDRLEELeERLLAALLALLPAELPPVLVHGDLHPGNLLVDPGG-RVSGVIDFEDAGLGDPAY 203
|
90 100
....*....|....*....|...
gi 1720414863 97 DVAYSCLAYYLPSSFPILRGFRD 119
Cdd:pfam01636 204 DLAILLNSWGRELGAELLAAYLA 226
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
364-658 |
1.90e-17 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 84.88 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 364 GNMEILVRYGTEEQKARWLVPLLEGRIRSCFAMTEPQvASSDASNIEASIKEEDGCYVINGHKWW-TSGILDPrckLCVF 442
Cdd:PRK03354 92 GGFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPG-AGSDVGSLKTTYTRRNGKVYLNGSKCFiTSSAYTP---YIVV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 443 MGKtDPQAPRHQQQSMLLVPMDSPGITViRPLSVFGLEdpPGGHGEVRFKDVRVPKENILLGPGRGF-----EIAQGRLG 517
Cdd:PRK03354 168 MAR-DGASPDKPVYTEWFVDMSKPGIKV-TKLEKLGLR--MDSCCEITFDDVELDEKDMFGREGNGFnrvkeEFDHERFL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 518 PGRIHHCMRLIGYsERALALMKTRVmsrtAFGKPLVEQGTILADIARSRVEIEQARLLVLKAAHLMDvAGNKTAAlDIAM 597
Cdd:PRK03354 244 VALTNYGTAMCAF-EDAARYANQRV----QFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKAD-NGTITSG-DAAM 316
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720414863 598 IKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALRFADGPDEVHQLTVAKMELK 658
Cdd:PRK03354 317 CKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLK 377
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
373-639 |
2.00e-12 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 69.27 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 373 GTEEQKARWLVPLLEGRIRSCfAMTEpqVASSDASNIEASIKEEDGCYVINGHKWWTSGILDprCKLCVFMGKTDPQAPR 452
Cdd:cd01163 87 GPEQFRKRWFGRVLNGWIFGN-AVSE--RGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALF--SDWVTVSALDEEGKLV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 453 HqqqsmLLVPMDSPGITVIRPLSVFGLEDPpgGHGEVRFKDVRVPKENILLGPGRGFeiaQGRLGPG--RIHHCMRLIGY 530
Cdd:cd01163 162 F-----AAVPTDRPGITVVDDWDGFGQRLT--ASGTVTFDNVRVEPDEVLPRPNAPD---RGTLLTAiyQLVLAAVLAGI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 531 SERALALMKTRVMSRT-AFGKPLVEQGT----ILADIARSRVEIEQARLLVLKAAHLMDVAGNK----------TAALDI 595
Cdd:cd01163 232 ARAALDDAVAYVRSRTrPWIHSGAESARddpyVQQVVGDLAARLHAAEALVLQAARALDAAAAAgtaltaeargEAALAV 311
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1720414863 596 AMIKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFfgWaRALR 639
Cdd:cd01163 312 AAAKVVVTRLALDATSRLFEVGGASATAREHNLDRH--W-RNAR 352
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
305-613 |
1.09e-10 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 64.98 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 305 DLKEKA----KAEGLWNLFLPletdpeKKYGaGLTNVEYAHLCEVMGMSLYASeifncSAPDT-------GNMEILVRYG 373
Cdd:PRK13026 108 DLPPEVwdylKKEGFFALIIP------KEYG-GKGFSAYANSTIVSKIATRSV-----SAAVTvmvpnslGPGELLTHYG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 374 TEEQKARWLVPLLEGRIRSCFAMTEPQvASSDASNI-EASI---KEEDGCYV----INGHKWWTSgiLDPRCK---LCVF 442
Cdd:PRK13026 176 TQEQKDYWLPRLADGTEIPCFALTGPE-AGSDAGAIpDTGIvcrGEFEGEEVlglrLTWDKRYIT--LAPVATvlgLAFK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 443 MgkTDP----QAPRHQQQSMLLVPMDSPGITVIR---PL-SVFgledppgGHGEVRFKDVRVPKENILLGP---GRGFEI 511
Cdd:PRK13026 253 L--RDPdgllGDKKELGITCALIPTDHPGVEIGRrhnPLgMAF-------MNGTTRGKDVFIPLDWIIGGPdyaGRGWRM 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 512 AQGRLGPGRihhcmrliGYSERALAL----MKTRVMS-----RTAFGKPL-----VEQGtiLADIARSRVEIEQARLLVl 577
Cdd:PRK13026 324 LVECLSAGR--------GISLPALGTasghMATRTTGayayvRRQFGMPIgqfegVQEA--LARIAGNTYLLEAARRLT- 392
|
330 340 350
....*....|....*....|....*....|....*..
gi 1720414863 578 kaahlmdvagnkTAALDIAMIKMVVPSMA-YHVIDRA 613
Cdd:PRK13026 393 ------------TTGLDLGVKPSVVTAIAkYHMTELA 417
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
523-639 |
5.33e-10 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 57.74 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 523 HCMRLIGYSERALA----LMKTRVmsRTAFGKPLVEQGTILADIARSRVEIEQARLLVLKAA--HLMDVAGNK--TAAL- 593
Cdd:pfam08028 2 IAAAALGAARAALAefteRARGRV--RAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAarIEAAAAAGKpvTPALr 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1720414863 594 -DIAMIKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARALR 639
Cdd:pfam08028 80 aEARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAA 126
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
366-553 |
4.40e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 59.10 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 366 MEILVRYGTEEQKARWLVPLLEGRIRSCFAMTEPQVAsSDASNIEASIKEEDGCYVINGHKWW--TSGILDprcKLCVFM 443
Cdd:PLN02526 118 MLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYG-SDASSLNTTATKVEGGWILNGQKRWigNSTFAD---VLVIFA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 444 GKTDPqaprhQQQSMLLVPMDSPGITVIRPLSVFGLEDPPggHGEVRFKDVRVPKENILlgPG-RGFEIAQGRLGPGRIH 522
Cdd:PLN02526 194 RNTTT-----NQINGFIVKKGAPGLKATKIENKIGLRMVQ--NGDIVLKDVFVPDEDRL--PGvNSFQDTNKVLAVSRVM 264
|
170 180 190
....*....|....*....|....*....|.
gi 1720414863 523 HCMRLIGYSERALALMKTRVMSRTAFGKPLV 553
Cdd:PLN02526 265 VAWQPIGISMGVYDMCHRYLKERKQFGAPLA 295
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
274-388 |
5.00e-09 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 54.39 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 274 QFIEQKVYPLEPEL-QRHQASADRWspspliedlkEKAKAEGLWNLFLPletdpeKKYG-AGLTNVEYAHLCEVMGMSLY 351
Cdd:pfam02771 13 EFAEEEIAPHAAEWdEEGEFPRELW----------KKLGELGLLGITIP------EEYGgAGLDYLAYALVAEELARADA 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1720414863 352 ASEIFnCSAPDTGNMEILVRYGTEEQKARWLVPLLEG 388
Cdd:pfam02771 77 SVALA-LSVHSSLGAPPILRFGTEEQKERYLPKLASG 112
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
311-409 |
9.85e-08 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 55.21 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 311 KAEGLWNLFLPletdpeKKYGaGLTNVEYAHLCEVM---GMSLYASeiFNCSAPDT-GNMEILVRYGTEEQKARWLVPLL 386
Cdd:PRK09463 119 KEHGFFGMIIP------KEYG-GLEFSAYAHSRVLQklaSRSGTLA--VTVMVPNSlGPGELLLHYGTDEQKDHYLPRLA 189
|
90 100
....*....|....*....|...
gi 1720414863 387 EGRIRSCFAMTEPQvASSDASNI 409
Cdd:PRK09463 190 RGEEIPCFALTSPE-AGSDAGSI 211
|
|
| CotS |
COG0510 |
Thiamine kinase or a related kinase [Coenzyme transport and metabolism]; |
29-108 |
2.31e-07 |
|
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
Pssm-ID: 440276 [Multi-domain] Cd Length: 156 Bit Score: 50.94 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 29 KQYRAAETSSIPAMERLIQWLPLHLPRQ-QRTTLVHGDFRLDNLIFHPEKAevLAVLDWELSTLGDPFADVAYSCLAYYL 107
Cdd:COG0510 18 ERYLALGPRDLPELLRRLEELERALAARpLPLVLCHGDLHPGNFLVTDDGR--LYLIDWEYAGLGDPAFDLAALLVEYGL 95
|
.
gi 1720414863 108 P 108
Cdd:COG0510 96 S 96
|
|
| APH_ChoK_like |
cd05120 |
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ... |
59-100 |
6.01e-07 |
|
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).
Pssm-ID: 270690 [Multi-domain] Cd Length: 158 Bit Score: 49.61 E-value: 6.01e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1720414863 59 TTLVHGDFRLDNLIFHPEKaEVLAVLDWELSTLGDPFADVAY 100
Cdd:cd05120 111 SVLTHGDLHPGNILVKPDG-KLSGIIDWEFAGYGPPAFDYAA 151
|
|
| SrkA |
COG2334 |
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ... |
21-118 |
7.93e-05 |
|
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 441905 [Multi-domain] Cd Length: 297 Bit Score: 44.92 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 21 PRQVQTWTKQYRAAETSSIPA-------------MERLIQWLPLHLPRQqrttLVHGDFRLDNLIFHPEKaeVLAVLDWE 87
Cdd:COG2334 132 ARDLAWWDELLERLLGPLLPDpedralleelldrLEARLAPLLGALPRG----VIHGDLHPDNVLFDGDG--VSGLIDFD 205
|
90 100 110
....*....|....*....|....*....|....*..
gi 1720414863 88 LSTLGDPFADVAYsCLAYYLPSSFP------ILRGFR 118
Cdd:COG2334 206 DAGYGPRLYDLAI-ALNGWADGPLDparlaaLLEGYR 241
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
364-637 |
5.96e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 42.93 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 364 GNMEILVRYGTEEQKARWLVPLLEGRIRSCFAMTEPQVASSDASNIEASIKEEDGCYVINGHKWW--------TSGILDp 435
Cdd:PTZ00456 155 GAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFisagdhdlTENIVH- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 436 rcklcVFMGKTDPQAPRHQQQSMLLVPMDSP----GITVIRPLSVFGLEDPPGGHG----EVRFKDvrvpKENILLG-PG 506
Cdd:PTZ00456 234 -----IVLARLPNSLPTTKGLSLFLVPRHVVkpdgSLETAKNVKCIGLEKKMGIKGsstcQLSFEN----SVGYLIGePN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 507 RGFEIAQGRLGPGRIHHCMRLIGYSERAL--ALMKTR-VMSRTAF---------GKPLVEQGTILADIARSRVEIEQARL 574
Cdd:PTZ00456 305 AGMKQMFTFMNTARVGTALEGVCHAELAFqnALRYAReRRSMRALsgtkepekpADRIICHANVRQNILFAKAVAEGGRA 384
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720414863 575 LVLKAAHLMDVAGN-KTAALDIAM----------IKMVVPSMAYHVIDRAIQAFGAAGLSSDYPLAQFFGWARA 637
Cdd:PTZ00456 385 LLLDVGRLLDIHAAaKDAATREALdheigfytpiAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARI 458
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
398-639 |
1.38e-03 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 41.57 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 398 EPQVASSDASNIEASIKEEDGCYVINGHKWWTSGILDPRCKLCVFM-----GKTDPQAprhqqqsmLLVPMDspGITVIR 472
Cdd:cd01159 98 GPDTLLAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIvedddGGPLPRA--------FVVPRA--EYEIVD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 473 PLSVFGLEDPpgGHGEVRFKDVRVPKENILL------GPGRGFEIAQGRLGPGRIH---HCMRLIGYSERALALM----K 539
Cdd:cd01159 168 TWHVVGLRGT--GSNTVVVDDVFVPEHRTLTagdmmaGDGPGGSTPVYRMPLRQVFplsFAAVSLGAAEGALAEFlelaG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720414863 540 TRVmSRTAFGKPLVEQGTILADIARSRVEIEQARLLVLKA-AHLMDVAGNKTAA---------LDIAMikmvVPSMAYHV 609
Cdd:cd01159 246 KRV-RQYGAAVKMAEAPITQLRLAEAAAELDAARAFLERAtRDLWAHALAGGPIdveerarirRDAAY----AAKLSAEA 320
|
250 260 270
....*....|....*....|....*....|
gi 1720414863 610 IDRAIQAFGAAGLSSDYPLAQFFGWARALR 639
Cdd:cd01159 321 VDRLFHAAGGSALYTASPLQRIWRDIHAAA 350
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|
| APH |
cd05150 |
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ... |
43-99 |
4.83e-03 |
|
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group from ATP to aminoglycoside antibiotics such as kanamycin, streptomycin, neomycin, and gentamicin, among others. The aminoglycoside antibiotics target the 30S ribosome and promote miscoding, leading to the production of defective proteins which insert into the bacterial membrane, resulting in membrane damage and the ultimate demise of the bacterium. Phosphorylation of the aminoglycoside antibiotics results in their inactivation, leading to bacterial antibiotic resistance. The APH gene is found on transposons and plasmids and is thought to have originated as a self-defense mechanism used by microorganisms that produce the antibiotics. The APH subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).
Pssm-ID: 270699 [Multi-domain] Cd Length: 244 Bit Score: 39.10 E-value: 4.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720414863 43 ERLIQWLPLHLPRQQRTTLVHGDFRLDNLIFHPEKaeVLAVLDWELSTLGDPFADVA 99
Cdd:cd05150 147 EELLAELEATRPAEEDLVVTHGDACLPNIILDPGR--FSGFIDLGRLGVADRYQDLA 201
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